ID   CHEA_LISMO              Reviewed;         618 AA.
AC   Q48768;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 2.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Chemotaxis protein cheA;
DE            EC=2.7.13.3;
GN   Name=cheA; OrderedLocusNames=lmo0692;
OS   Listeria monocytogenes.
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=12067;
RX   MEDLINE=95102110; PubMed=7803815;
RA   Dons L., Olsen J.E., Rasmussen O.F.;
RT   "Characterization of two putative Listeria monocytogenes genes
RT   encoding polypeptides homologous to the sensor protein CheA and the
RT   response regulator CheY of chemotaxis.";
RL   DNA Seq. 4:301-311(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e / Serovar 1/2a;
RX   MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA   Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA   Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA   Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA   Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA   Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- FUNCTION: Involved in the transmission of sensory signals from the
CC       chemoreceptors to the flagellar motors. CheA is
CC       autophosphorylated; it can transfer its phosphate group to either
CC       cheB or cheY (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Contains 1 cheW-like domain.
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
CC   -!- SIMILARITY: Contains 1 HPt domain.
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DR   EMBL; X76170; CAA53765.1; -; Genomic_DNA.
DR   EMBL; AL591976; CAC98770.1; -; Genomic_DNA.
DR   PIR; AD1161; AD1161.
DR   RefSeq; NP_464219.1; -.
DR   HSSP; Q56310; 1I58.
DR   GeneID; 985032; -.
DR   GenomeReviews; AL591824_GR; lmo0692.
DR   KEGG; lmo:lmo0692; -.
DR   ListiList; LMO00692; -.
DR   HOGENOM; Q48768; -.
DR   OMA; Q48768; ATSERRY.
DR   BioCyc; LMON169963:LMO0692-MON; -.
DR   BRENDA; 2.7.13.3; 96770.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0006928; P:cell motion; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0018106; P:peptidyl-histidine phosphorylation; IEA:InterPro.
DR   GO; GO:0000160; P:two-component signal transduction system (p...; IEA:UniProtKB-KW.
DR   InterPro; IPR003594; ATP_bd_ATPase.
DR   InterPro; IPR002545; CheW.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_P-trf.
DR   InterPro; IPR004105; Sig_transdc_His_kin_subgr_dim.
DR   InterPro; IPR005467; Sig_transdc_His_kinase_core.
DR   InterPro; IPR010808; Sig_transdc_His_kinase_P2-bd.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF07194; P2; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   ProDom; PD003142; Hpt_N; 1.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chemotaxis; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase;
KW   Two-component regulatory system.
FT   CHAIN         1    618       Chemotaxis protein cheA.
FT                                /FTId=PRO_0000074715.
FT   DOMAIN        1    102       HPt.
FT   DOMAIN      233    488       Histidine kinase.
FT   DOMAIN      490    618       CheW-like.
FT   MOD_RES      45     45       Phosphohistidine; by autocatalysis (By
FT                                similarity).
FT   CONFLICT    132    132       T -> A (in Ref. 1; CAA53765).
FT   CONFLICT    140    140       A -> Q (in Ref. 1; CAA53765).
FT   CONFLICT    197    197       D -> E (in Ref. 1; CAA53765).
FT   CONFLICT    200    200       K -> E (in Ref. 1; CAA53765).
FT   CONFLICT    203    203       I -> V (in Ref. 1; CAA53765).
SQ   SEQUENCE   618 AA;  68628 MW;  63B560C05D8E941C CRC64;
     MTTNMLDLFI EEASEHLQAL NDNLLQLEKD PTNGQLVSEI FRSAHTFKGM SATMGFQQVA
     DLTHAMENVL DEVRNNRLAV TEHLVDIIFT CTSHLETMVS DIQHGGQGAA DISKTVADLE
     ALLHPEQETD LTVEKTYRIA IQIEEAAILK AVRAVMCLER LAEMGIISET TPDREAIELE
     EFEQSFEVVL ESAQTKDEIK AVILDISEIE KVTVTEEVEE VQVIEPIKKA AKQTTKRLEN
     KTIRVQLEKI EKLMNVFEES VIERARIDEI AEKTNNKELM EHLGRFSSIS KEIQNGLLNM
     RMVPVDSVFN RFPKMVRTLA KELGKKIDLV IEGADTEVDK IVIDEIGDPL VHLIRNSVDH
     GAETVEVRRK NGKNETATIN LKAFHSGNNV VIEIADDGAG INKRKVLEKA IAKNVVTRAE
     STKMTDAEIF DLLFDSGFST ADQVSDLSGR GVGLDVVRNT ILKIGGKISV ESSENAGSTF
     RIEIPLTLSI IQSMLVATSE RRYAVPLANV AEAITINPAD IQHVHGKDLI NYRETIIEVL
     DLGECFHETP LNDTDELLLL VVKNAKRTFG LIIKDIIGQR EIVLKTLGGF FSESQIAFSG
     ATILGDGRVV LILNLETF
//